Reviewed, UniProtKB/Swiss-Prot P57472 (PHEA_BUCAI)

Names and origin

Protein names

Recommended name:
    P-protein
Including the following 2 domains:
    1- Recommended name:
            Chorismate mutase
                Short name=CM
              EC=5.4.99.5
    2- Recommended name:
            Prephenate dehydratase
                Short name=PDT
              EC=4.2.1.51

Gene names

Name:	pheA
Synonyms:	aroQ/pheA
Ordered Locus Names:	BU392

Organism

Buchnera aphidicola subsp. Acyrthosiphon pisum (Acyrthosiphon pisum symbiotic bacterium) [Complete proteome] [HAMAP]

Taxonomic identifier

118099 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Buchnera

Protein attributes

Sequence length	385 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Predicted.

General annotation (Comments)

Catalytic activity	Chorismate = prephenate. Prephenate = phenylpyruvate + H2O + CO2.
Pathway	Amino-acid biosynthesis; L-phenylalanine biosynthesis; phenylpyruvate from prephenate: step 1/1. Metabolic intermediate biosynthesis; prephenate biosynthesis; prephenate from chorismate: step 1/1.
Subcellular location	Cytoplasm.
Domain	The regulatory domain shows changes in the ESRP sequence, which is involved in the allosteric binding of phenylalanine. These changes suggest the desensitization of the enzyme to inhibition by phenylalanine and would permit the overproduction of phenylalanine.
Sequence similarities	Contains 1 chorismate mutase domain. Contains 1 prephenate dehydratase domain.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Aromatic amino acid biosynthesis Phenylalanine biosynthesis
Cellular component	Cytoplasm
Molecular function	Isomerase Lyase
Technical term	Allosteric enzyme Complete proteome Multifunctional enzyme
Gene Ontology (GO)
Biological process	L-phenylalanine biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	chorismate mutase activity Inferred from electronic annotation. Source: EC prephenate dehydratase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 385	385	P-protein		PRO_0000119182
Regions
	Domain	1 – 92	92	Chorismate mutase
	Domain	105 – 285	181	Prephenate dehydratase
	Region	286 – 385	100	Regulatory
Sites
	Site	278	1	Essential for prephenate dehydratase activity Potential

Sequences

	Sequence		Length	Mass (Da)
	P57472-1 [UniParc]. Last modified December 1, 2000. Version 1. Checksum: 7EFD783A4C62F9E7	FASTA	385	44,338
	10 20 30 40 50 60 MPANNSLLIF RDEINNIDKK IVKLLAERKN LVFKIAQSKI ENNQAIRDIE REKKMLQKLI 70 80 90 100 110 120 FLGKKYNLKS EYITQLFQLI IEESVATQKK LLKKFCNHNK LIPANFSFLG PKGSYSHIAA 130 140 150 160 170 180 YKYADLNFQK CITNECSTFE EVVLSVENNQ SDYAVLPIEN TCSGSINEVF DILKKTNLFI 190 200 210 220 230 240 IGEINIFINH NLLTLKKIEL NKIKTIYSHP QPFQQCSDFI KKFPEWKIKY TKSTADAMKK 250 260 270 280 290 300 IKKYNDVTNA ALGSEIGSKI YGLEILMKNL ANKENNITRF ILLNRNPKKI SKNIPTTTTL 310 320 330 340 350 360 IFTTGQEAGS LSKVLSILQE KKLIMKKLTS QKIYKNPWEE MFYIDIQVNL SSTLMQDALE 370 380 KIKKITRFIK ILGCYPSEKI TPIAP

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Prephenate dehydratase from the aphid endosymbiont (Buchnera) displays changes in the regulatory domain that suggest its desensitization to inhibition by phenylalanine." Jimenez N., Gonzalez-Candelas F., Silva F.J. J. Bacteriol. 182:2967-2969(2000) [PubMed: 10781569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS." Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H. Nature 407:81-86(2000) [PubMed: 10993077] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Tokyo 1998.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AJ239043 Genomic DNA. Translation: CAB90996.1. BA000003 Genomic DNA. Translation: BAB13095.1.
RefSeq	NP_240209.1.
3D structure databases
HSSP	HSSP built from PDB template 1ECM based on UniProtKB P07022.
ModBase	Search...
Genome annotation databases
GeneID	1109745.
GenomeReviews	Gene locus BU392 in contig BA000003_GR.
KEGG	buc:BU392.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	P57472.
OMA	P57472. TLYSHPQ.
Enzyme and pathway databases
BioCyc	BSP107806:BU392-MON.
BRENDA	4.2.1.51. 118624.
Family and domain databases
InterPro	IPR008242. Chor_mutase/pphenate_deHydtase. IPR002701. Chorismate_mut. IPR010952. CM_P_1. IPR001086. Preph_deHydtase. IPR018528. Preph_deHydtase_CS. [Graphical view]
Pfam	PF01817. CM_2. 1 hit. PF00800. PDT. 1 hit. [Graphical view]
PIRSF	PIRSF001500. Chor_mut_pdt_Ppr. 1 hit.
TIGRFAMs	TIGR01797. CM_P_1. 1 hit.
PROSITE	PS51168. CHORISMATE_MUT_2. 1 hit. PS00857. PREPHENATE_DEHYDR_1. 1 hit. PS00858. PREPHENATE_DEHYDR_2. False negative. PS51171. PREPHENATE_DEHYDR_3. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

PHEA_BUCAI

Accession

Primary (citable) accession number: P57472
Secondary accession number(s): Q9L4J2

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	December 1, 2000
Last modified:	June 16, 2009
This is version 66 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)